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Titolo:
Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides
Autore:
Miyagi, T; Wada, T; Iwamatsu, A; Hata, K; Yoshikawa, Y; Tokuyama, S; Sawada, M;
Indirizzi:
Miyagi Prefectural Canc Ctr, Res Inst, Div Biochem, Natori, Miyagi 9811293, Miyagi Prefectural Canc Ctr Natori Miyagi Japan 9811293 , Miyagi 9811293, Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa 236, JapanKirin Brewery Co Ltd Yokohama Kanagawa Japan 236 ama, Kanagawa 236, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 8, volume: 274, anno: 1999,
pagine: 5004 - 5011
SICI:
0021-9258(19990219)274:8<5004:MCACOA>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN NEUROBLASTOMA-CELLS; CYTOSOLIC SIALIDASE; GROWTH-CONTROL; GM3 GANGLIOSIDE; MESSENGER-RNA; GENE-TRANSFER; RAT-LIVER; DIFFERENTIATION; FIBROBLASTS; ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Miyagi, T Miyagi Prefectural Canc Ctr, Res Inst, Div Biochem, Natori, Miyagi 9811293, Miyagi Prefectural Canc Ctr Natori Miyagi Japan 9811293 811293,
Citazione:
T. Miyagi et al., "Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides", J BIOL CHEM, 274(8), 1999, pp. 5004-5011

Abstract

Gangliosides are plasma membrane components thought to play important roles in cell surface interactions, cell differentiation, and transmembrane signaling. A mammalian sialidase located in plasma membranes is unique in specifically hydrolyzing gangliosides, suggesting crucial roles in regulation of cell surface functions. Here we describe the cloning and expression of a cDNA for the ganglioside sialidase, isolated from a bovine brain cDNA library based on the amino acid sequence of the purified enzyme from bovine brain. This cDNA encodes a 428-amino acid protein containing a putative transmembrane domain and the three Asp boxes characteristic of sialidases and sharing 19-38% sequence identity with other sialidases, Northern blot and polymerase chain reaction analyses revealed a general distribution of the gene in mammalian species, including man, and the mouse. In COS-7 cells transiently expressing the sialidase, the activity was found to be 40-fold that of the control level with ganglioside substrates in the presence of Triton X-100, and the hydrolysis was almost specific to gangliosides other than GM1 and GM2, both alpha 2-->3 and alpha 2-->8 sialyl linkages being susceptible. The major subcellular localization of the expressed sialidase was assessed to be plasma membrane by Percoll density gradient centrifugation of cell homogenates and by immunofluorescence staining of the transfected COS-7 cells. Analysis of the membrane topology by protease protection assay suggested that this sialidase has a type I membrane orientation with its amino terminus facing to the extracytoplasmic side and lacking a signal sequence.

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Documento generato il 15/01/21 alle ore 22:59:37